Collagenase is a protease which cleaves the triple-helical protein called collagen

• Presentation: Brown Lyophilized Powder
• Dissolve enzyme at a concentration of 1 mg/mL in 0.05 M TES with 0.36 mM calcium chloride, pH 7.5.

Collagenase from Clostridium histolyticum has extensive use in biological studies, where it is used to prepare isolated cell suspensions.

Collagenase is activated by four gram atom calcium per mole enzyme. It is inhibited by ethylene glycol-bis(beta-aminoethyl ether) - N, N, N′,N′-tetraacetic acid, beta-mercaptoethanol, glutathione, thioglycolic acid and 8-hydroxyquinoline.

The collagenase product is a mixture of enzymes secreted by C. histolyticum, with different products differentiated by the relative ratios of the 10-18 components found in the secreted enzymes. The main components are two collagenases, clostripain, and a neutral protease. The synergistic action of these enzymes degrade collagen and other intracellular material. The action of both collagenase enzymes and the neutral protease is necessary for effective release of cells from tissue. Various types of collagen are the natural substrates for collagenase.

There are three types of tissue collagenases, and these belong to the matrix metalloproteinases (MMP) family.